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Cost-Effective Production and Optimization of Alkaline Xylanase by Indigenous Bacillus mojavensis AG137 Fermented on Agricultural Waste
A xylanase producer Bacillus mojavensis strain, called AG137, isolated from cotton farm (Kashan-Iran). The optimal xylanase activity reached at 55°C & pH 9.0. Enzyme yield was studied using a medium with different agricultural wastes as inducers. Xylanase production of about 249.308 IU/mL was ac...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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SAGE-Hindawi Access to Research
2011
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3166571/ https://www.ncbi.nlm.nih.gov/pubmed/21904670 http://dx.doi.org/10.4061/2011/593624 |
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author | Akhavan Sepahy, Abbas Ghazi, Shokoofeh Akhavan Sepahy, Maryam |
author_facet | Akhavan Sepahy, Abbas Ghazi, Shokoofeh Akhavan Sepahy, Maryam |
author_sort | Akhavan Sepahy, Abbas |
collection | PubMed |
description | A xylanase producer Bacillus mojavensis strain, called AG137, isolated from cotton farm (Kashan-Iran). The optimal xylanase activity reached at 55°C & pH 9.0. Enzyme yield was studied using a medium with different agricultural wastes as inducers. Xylanase production of about 249.308 IU/mL was achieved at pH 8 and 37°C, within 48 h submerged fermentation in enzyme production medium supplemented with 2% (w/v) oat bran as an optimum carbon source. A mixture of 1% (w/v) yeast extract and 1% (w/v) tryptone as optimum nitrogen sources, agitation speed 200 rpm, and inoculum size 2% (v/v) were the optimums for maximum production. Accordingly, xylanase yield from 194.68 IU/mL under non-optimized fermentation condition enhanced to 302.466 IU/mL in optimized condition. Screened xylanase is thermostable, presenting 70% stability at 60°C during 30 min. Further enzyme incubation in higher temperature caused a decrease in the residual enzyme activity, yet it retained 68%–50% of its activity after 1 hour from 45°C to 55°C. Besides, it is stable in pH 9 and 10, maintaining over 70% of its activity for 2 h. The enzyme also could preserve 71% and 63% of its initial activity after 3 hours of pre-incubation in the same alkaline condition. Produced xylanase therefore was introduced as an alkaline-active and stable one, displaying suitable thermostability feature, confirmed by HPLC analysis. Hence, all xylanase properties highlight its promising uses in industrial scale. |
format | Online Article Text |
id | pubmed-3166571 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | SAGE-Hindawi Access to Research |
record_format | MEDLINE/PubMed |
spelling | pubmed-31665712011-09-08 Cost-Effective Production and Optimization of Alkaline Xylanase by Indigenous Bacillus mojavensis AG137 Fermented on Agricultural Waste Akhavan Sepahy, Abbas Ghazi, Shokoofeh Akhavan Sepahy, Maryam Enzyme Res Research Article A xylanase producer Bacillus mojavensis strain, called AG137, isolated from cotton farm (Kashan-Iran). The optimal xylanase activity reached at 55°C & pH 9.0. Enzyme yield was studied using a medium with different agricultural wastes as inducers. Xylanase production of about 249.308 IU/mL was achieved at pH 8 and 37°C, within 48 h submerged fermentation in enzyme production medium supplemented with 2% (w/v) oat bran as an optimum carbon source. A mixture of 1% (w/v) yeast extract and 1% (w/v) tryptone as optimum nitrogen sources, agitation speed 200 rpm, and inoculum size 2% (v/v) were the optimums for maximum production. Accordingly, xylanase yield from 194.68 IU/mL under non-optimized fermentation condition enhanced to 302.466 IU/mL in optimized condition. Screened xylanase is thermostable, presenting 70% stability at 60°C during 30 min. Further enzyme incubation in higher temperature caused a decrease in the residual enzyme activity, yet it retained 68%–50% of its activity after 1 hour from 45°C to 55°C. Besides, it is stable in pH 9 and 10, maintaining over 70% of its activity for 2 h. The enzyme also could preserve 71% and 63% of its initial activity after 3 hours of pre-incubation in the same alkaline condition. Produced xylanase therefore was introduced as an alkaline-active and stable one, displaying suitable thermostability feature, confirmed by HPLC analysis. Hence, all xylanase properties highlight its promising uses in industrial scale. SAGE-Hindawi Access to Research 2011 2011-08-29 /pmc/articles/PMC3166571/ /pubmed/21904670 http://dx.doi.org/10.4061/2011/593624 Text en Copyright © 2011 Abbas Akhavan Sepahy et al. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Article Akhavan Sepahy, Abbas Ghazi, Shokoofeh Akhavan Sepahy, Maryam Cost-Effective Production and Optimization of Alkaline Xylanase by Indigenous Bacillus mojavensis AG137 Fermented on Agricultural Waste |
title | Cost-Effective Production and Optimization of Alkaline Xylanase by Indigenous Bacillus mojavensis AG137 Fermented on Agricultural Waste |
title_full | Cost-Effective Production and Optimization of Alkaline Xylanase by Indigenous Bacillus mojavensis AG137 Fermented on Agricultural Waste |
title_fullStr | Cost-Effective Production and Optimization of Alkaline Xylanase by Indigenous Bacillus mojavensis AG137 Fermented on Agricultural Waste |
title_full_unstemmed | Cost-Effective Production and Optimization of Alkaline Xylanase by Indigenous Bacillus mojavensis AG137 Fermented on Agricultural Waste |
title_short | Cost-Effective Production and Optimization of Alkaline Xylanase by Indigenous Bacillus mojavensis AG137 Fermented on Agricultural Waste |
title_sort | cost-effective production and optimization of alkaline xylanase by indigenous bacillus mojavensis ag137 fermented on agricultural waste |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3166571/ https://www.ncbi.nlm.nih.gov/pubmed/21904670 http://dx.doi.org/10.4061/2011/593624 |
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